Characterization of a subunit structure and stability of the recombinant porin from Neisseria gonorrhoeae

Journal of Protein Chemistry

Volumn 17, Issue 7, 1998, Pages 719-728

  Matsuka, Yury V ^a   Dilts, Deborah A ^a   Hoiseth, Susan ^a   Arumugham, Rasappa ^a  

^a PFIZER INC   (United States)

Author keywords

ANS; Expression; Intermediate state; N. gonorrhoeae porin; Unfolding

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; AMPHOLYTE; GUANIDINE; MONOMER; OLIGOMER; OUTER MEMBRANE PROTEIN; PORIN; PROTEIN SUBUNIT; RECOMBINANT PROTEIN;

ARTICLE; CONTROLLED STUDY; ESCHERICHIA COLI; FLUORESCENCE SPECTROSCOPY; GEL PERMEATION CHROMATOGRAPHY; HEATING; HYDROPHOBICITY; NEISSERIA GONORRHOEAE; NONHUMAN; PROTEIN ANALYSIS; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE;

ESCHERICHIA COLI; NEISSERIA GONORRHOEAE;

EID: 0031761882     PISSN: 02778033     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02780975     Document Type: Article

References (34)

1. Blake, M. S., and Gotschlich, E. S. (1982). Infect. Immun. 36, 277-283.
2. Butt, N. J., Lambden, P. R., and Heckels, J. E. (1990). Nucleic Acids Res. 18, 4258.
3. Carbonetti, N. H., and Sparling, P. F. (1987). Proc. Natl. Acad. Sci. USA 84, 9084-9088.
4. Carbonetti, N. H., Simnad, V. I., Seifert, H. S., So, M., and Sparling, P. F. (1988). Proc. Natl. Acad. Sci. USA 85, 6841-6845.
5. Cleary, S., Mulkerrin, M. G., and Kelley, R. F. (1989). Biochemistry 28, 1884-1891.
6. Cowan, S. W., Schirmer, T., Rummel, G., Steiert, M., Ghosh, R., Pauptit, R. A., Jansonius, J. N., and Rosenbusch, J. P. (1992). Nature 358, 727-733.
7. Douglas, J. T., Lee, M. D., and Nikaido, H. (1981). FEMS Microbiol. Lett. 12, 305-309.
8. Edelhoch, H. (1967). Biochemistry 6, 1948-1954.
9. Ferguson, R. N., and Cahnmann, H. J. (1975). Biochemistry 14, 282-289.
10. Gotschlich, E. C., Seiff, M. E., Blake, M. S., and Koomey, M. (1987). Proc. Natl. Acad. Sci. USA 84, 8135-8139.
11. Hancock, R. E. W. (1987). In Bacterial Outer Membranes as Model Systems, Wiley, New York.
12. Jaenicke, R. (1987). Prog. Biophys. Mol. Biol. 49, 117-237.
13. Jaenicke, R., and Rudolph, R. (1986). Meth. Enzymol. 131, 218-250.
14. Judd, R. C. (1989). Clin. Microbiol. Rev. 2, S41-S48.
15. Kreusch, A., Neubuser, A., Schiltz, E., Weckesser, J., and Schulz, G. E. (1994). Protein Sci. 3, 58-63.
16. Lakowicz, J. R. (1983). In Principles of Fluorescence Spectroscopy, Plenum Press, New York.
17. Markovic-Housley, Z., and Garavito, R. M. (1986). Biochim. Biophys. Acta 869, 158-170.
18. Matsuka, Y. V., Medved, L. V., Brew, S. A., and Ingham, K. C. (1994). J. Biol. Chem. 269, 9539-9546.
19. Mauro, A., Blake, M., and Labarca, P. (1988). Proc. Natl. Acad. Sci. USA 85, 1071-1075.
20. McDade, R. L., and Johnston, K. H. (1980). J. Bacteriol. 141, 1183-1191.
21. Minetti, C. A. S. A., Tai, J. Y., Blake, M. S., Pullen, J. K., Liang, S., and Remeta, D. P. (1997). J. Biol. Chem. 272, 10710-10720.
22. Nikaido, H. (1994). J. Biol. Chem. 269, 3905-3908.
23. Pace, N. C., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995). Protein Sci. 4, 2411-2423.
24. Puohiniemi, R., Butcher, S., Tarkka, E., and Sarvas, M. (1991). FEMS Microbiol. Lett. 83, 29-33.
25. Qi, H. L., Tai, J. Y., and Blake, M. S. (1994). Infect. Immun. 62, 2432-2439.
26. Schirmer, T., Keller, T. A., Wang, Y., and Rosenbusch, J. P. (1995). Science 267, 512-514.
27. Schmid, B., Kromer, M., and Schulz, G. E. (1996). FEBS Lett. 381, 111-114.
28. Schulz, G. E. (1996). Curr. Opin. Struct. Biol. 6, 485-490.
29. Seed, B. (1987). Nature 329, 840-842.
30. Semisotnov, G. V., Rodionova, N. A., Razgulyaev, O. I., Uversky, V. N., Gripas, A. F., and Gilmanshin, R. I. (1991). Biopolymers 31, 119-128.
31. Surrey, T., and Jahnig, F. (1995). J. Biol. Chem. 270, 28199-28203.
32. Weiss, M. F., and Schulz. G. E. (1992). J. Mol. Biol. 227, 493-509.
33. Wetzler, L. M., Blake, M. S., and Gotschlich, E. C. (1988). J. Exp. Med. 168, 1883-1897.
34. Young, J. D., Blake, M., Mauro, A., and Cohn, Z. (1983). Proc. Natl. Acad. Sci. USA 80, 3831-3835.